PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22610100-7	2012	This cleavage is tPA-specific, plasmin-independent, and removes a predicted ~4-kDa fragment (Arg(27)-Arg(67)) from the amino-terminal domain of the NR2B protein.	Arginine	93-96	plasminogen	Homo sapiens	31-38	
27797450-5	2016	SUMMARY: Background Using tissue factor pathway inhibitor (TFPI)-2 Kunitz domain1 (KD1), we obtained a bifunctional antifibrinolytic molecule (KD1L17R -KT ) with C-terminal lysine (kringle domain binding) and P2"-residue arginine (improved specificity towards plasmin).	Arginine	221-229	plasminogen	Homo sapiens	260-267	
25937317-3	2015	Proteins enriched in lysine and other positively charged residues (histidine and arginine) as well as glycosaminoglycans and gangliosides bind Plg.	Arginine	81-89	plasminogen	Homo sapiens	143-146	
22610100-7	2012	This cleavage is tPA-specific, plasmin-independent, and removes a predicted ~4-kDa fragment (Arg(27)-Arg(67)) from the amino-terminal domain of the NR2B protein.	Arginine	101-104	plasminogen	Homo sapiens	31-38	
17989726-7	2008	Predominant inhibition by LEKTI domains against overall SC protease activities was trypsin-like (Phe-Ser-Arg-) activity by LEKTI domains 6-12, plasmin- and trypsin-like (Pro-Phe-Arg-) activities by domains 12-15, chymotrypsin-like activity by all domains, and furin-like activity by none.	Arginine	105-108	plasminogen	Homo sapiens	143-150	
22079445-4	2012	MATERIALS AND METHODS: Compounds X-D-Arg-D-Phe-OMe, where X=residue of lauric or myristic acid or 9-fluorenylmethoxycarbonyl, have been synthesized by conventional peptide synthesis in solution and their comparative inhibitory analysis in relation to thrombin, factor X, plasmin and trypsin has been conducted.	Arginine	37-40	plasminogen	Homo sapiens	271-278	
17989726-7	2008	Predominant inhibition by LEKTI domains against overall SC protease activities was trypsin-like (Phe-Ser-Arg-) activity by LEKTI domains 6-12, plasmin- and trypsin-like (Pro-Phe-Arg-) activities by domains 12-15, chymotrypsin-like activity by all domains, and furin-like activity by none.	Arginine	178-181	plasminogen	Homo sapiens	143-150	
16087677-0	2005	Plasmin- and thrombin-accelerated shedding of syndecan-4 ectodomain generates cleavage sites at Lys(114)-Arg(115) and Lys(129)-Val(130) bonds.	Arginine	105-108	plasminogen	Homo sapiens	0-7	
17189254-5	2007	SDS-PAGE analysis showed that plasmin cleaved the heavy chain of factor VIII into two terminal products, A1(37-336) and A2 subunits, by limited proteolysis at Lys(36), Arg(336), Arg(372), and Arg(740).	Arginine	168-171	plasminogen	Homo sapiens	30-37	
17189254-5	2007	SDS-PAGE analysis showed that plasmin cleaved the heavy chain of factor VIII into two terminal products, A1(37-336) and A2 subunits, by limited proteolysis at Lys(36), Arg(336), Arg(372), and Arg(740).	Arginine	178-181	plasminogen	Homo sapiens	30-37	
17189254-5	2007	SDS-PAGE analysis showed that plasmin cleaved the heavy chain of factor VIII into two terminal products, A1(37-336) and A2 subunits, by limited proteolysis at Lys(36), Arg(336), Arg(372), and Arg(740).	Arginine	178-181	plasminogen	Homo sapiens	30-37	
17189254-7	2007	Plasmin-catalyzed cleavage at Arg(336) proceeded faster than that at Arg(372), in contrast to proteolysis by factor Xa.	Arginine	30-33	plasminogen	Homo sapiens	0-7	
17189254-7	2007	Plasmin-catalyzed cleavage at Arg(336) proceeded faster than that at Arg(372), in contrast to proteolysis by factor Xa.	Arginine	69-72	plasminogen	Homo sapiens	0-7	
17189254-10	2007	These results strongly indicated that cleavage at Arg(336) was a central mechanism of plasmin-catalyzed factor VIII inactivation.	Arginine	50-53	plasminogen	Homo sapiens	86-93	
17189254-11	2007	Furthermore, the cleavages at Arg(336) and Lys(36) appeared to be selectively regulated by the A2 and A3-C1-C2 domains, respectively, interacting with plasmin.	Arginine	30-33	plasminogen	Homo sapiens	151-158	
16708124-3	2006	These artefactual changes of PA or plasmin activities have been prevented by arginine stabilization of blood samples of myocardial infarction patients treated with plasminogen activators.	Arginine	77-85	plasminogen	Homo sapiens	35-42	
16708124-10	2006	Arginine stabilization of blood allows reliable determinations of activities of plasmin and PA in blood of patients under fibrinolytic treatment: substantial plasmin activities occur in patients treated by reteplase.	Arginine	0-8	plasminogen	Homo sapiens	80-87	
16708124-10	2006	Arginine stabilization of blood allows reliable determinations of activities of plasmin and PA in blood of patients under fibrinolytic treatment: substantial plasmin activities occur in patients treated by reteplase.	Arginine	0-8	plasminogen	Homo sapiens	158-165	
14567541-2	2003	Once activated, by thrombin or plasmin, TAFI down regulates fibrinolysis, slowing clot lysis by cleaving the C-terminal lysine and arginine residues from partially degraded fibrin.	Arginine	131-139	plasminogen	Homo sapiens	31-38	
16015416-0	2005	Functional determination of plasmin in arginine-stabilized plasma.	Arginine	39-47	plasminogen	Homo sapiens	28-35	
16015416-7	2005	For optimization of plasmin activity, the oxidation time of the arginine-stabilized plasma sample containing 0.5 U/mL active plasmin and the chloramine-T amount was varied.	Arginine	64-72	plasminogen	Homo sapiens	20-27	
16015416-7	2005	For optimization of plasmin activity, the oxidation time of the arginine-stabilized plasma sample containing 0.5 U/mL active plasmin and the chloramine-T amount was varied.	Arginine	64-72	plasminogen	Homo sapiens	125-132	
16015416-10	2005	The optimized functional plasmin assay consists of incubation of 10 microL arginine-stabilized plasma with 10 microL 1.5 M arginine, pH 8.7, and 10 microL 100 mM CT in PBS.	Arginine	75-83	plasminogen	Homo sapiens	25-32	
16015416-12	2005	With the present arginine stabilization procedure of plasma and the determination of plasmin activity in arginine-stabilized plasma as described, it is feasible to determine the activity of plasmin in blood of patients receiving fibrinolytic treatment without artefactual in vitro changes in the samples.	Arginine	17-25	plasminogen	Homo sapiens	190-197	
16015416-12	2005	With the present arginine stabilization procedure of plasma and the determination of plasmin activity in arginine-stabilized plasma as described, it is feasible to determine the activity of plasmin in blood of patients receiving fibrinolytic treatment without artefactual in vitro changes in the samples.	Arginine	105-113	plasminogen	Homo sapiens	85-92	
16015416-12	2005	With the present arginine stabilization procedure of plasma and the determination of plasmin activity in arginine-stabilized plasma as described, it is feasible to determine the activity of plasmin in blood of patients receiving fibrinolytic treatment without artefactual in vitro changes in the samples.	Arginine	105-113	plasminogen	Homo sapiens	190-197	
12924019-5	2002	Both 10(-2) M 6-aminohexanoic acid and 10(-1) M arginine reduced the complex formation rate between plasmin, mini-plasmin and alpha 2-antiplasmin to the value of the rate reaction between micro-plasmin and inhibitor.	Arginine	48-56	plasminogen	Homo sapiens	100-107	
12924019-5	2002	Both 10(-2) M 6-aminohexanoic acid and 10(-1) M arginine reduced the complex formation rate between plasmin, mini-plasmin and alpha 2-antiplasmin to the value of the rate reaction between micro-plasmin and inhibitor.	Arginine	48-56	plasminogen	Homo sapiens	114-121	
12924019-5	2002	Both 10(-2) M 6-aminohexanoic acid and 10(-1) M arginine reduced the complex formation rate between plasmin, mini-plasmin and alpha 2-antiplasmin to the value of the rate reaction between micro-plasmin and inhibitor.	Arginine	48-56	plasminogen	Homo sapiens	114-121	
10873770-5	2000	Mutation of Arg-340/Ser-341 at the predicted P1/P1" sites within the RCL prevented the formation of complexes between SPI-3 and plasmin, uPA, or tPA, suggesting that the arginine at the P1 position was required for complex formation.	Arginine	12-15	plasminogen	Homo sapiens	128-135	
11369771-1	2001	Cleavage of Arg(561)-Val(562) in plasminogen (Pg) generates plasmin (Pm) through a classical activation mechanism triggered by an insertion of the new amino terminus into a binding pocket in the Pg catalytic domain.	Arginine	12-15	plasminogen	Homo sapiens	33-40	
12022872-3	2002	Upon incubation with plasmin, TAFIa activity was generated, which was unstable at 37 degrees C. Analysis of the cleavage pattern showed that TAFI was cleaved at Arg(92), releasing the activation peptide from the 35.8-kDa catalytic domain.	Arginine	161-164	plasminogen	Homo sapiens	21-28	
11724583-1	2001	Plasmin (Pm), the main fibrinolytic protease in the plasma, is derived from its zymogen plasminogen (Plg) by cleavage of a peptide bond at Arg(561)-Val(562).	Arginine	139-142	plasminogen	Homo sapiens	88-99	
11724583-1	2001	Plasmin (Pm), the main fibrinolytic protease in the plasma, is derived from its zymogen plasminogen (Plg) by cleavage of a peptide bond at Arg(561)-Val(562).	Arginine	139-142	plasminogen	Homo sapiens	101-104	
10873770-5	2000	Mutation of Arg-340/Ser-341 at the predicted P1/P1" sites within the RCL prevented the formation of complexes between SPI-3 and plasmin, uPA, or tPA, suggesting that the arginine at the P1 position was required for complex formation.	Arginine	170-178	plasminogen	Homo sapiens	128-135	
10873836-6	2000	Plasmin achieves this unexpected, large differential activity even though both target sequences possess an arginine residue in the P1 position.	Arginine	107-115	plasminogen	Homo sapiens	0-7	
10496984-0	1999	Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin.	Arginine	124-132	plasminogen	Homo sapiens	251-258	
10896248-5	2000	In contrast, plasmin cleaves Tpo sequentially at two specific sites (Arg(205) within the glycan domain followed by Lys(52) within the cytokine domain), and is associated with a marked decrease in Tpo activity.	Arginine	69-72	plasminogen	Homo sapiens	13-20	
10585738-3	1999	The plasmin formed from plasminogen by the activators catalyzes the decomposition of the arginine-rich protamine substrate, yielding smaller polycationic fragments that are not sensed by the electrode.	Arginine	89-97	plasminogen	Homo sapiens	4-11	
10556566-2	1999	Cleavage of the Arg(561)-Val(562) activation site in plasminogen by either tissue- or urokinase-type plasminogen activator results in formation of the fibrinolytic enzyme plasmin.	Arginine	16-19	plasminogen	Homo sapiens	53-60	
9923600-4	1999	Plasmin cleaves gp160 precisely at the C-terminal arginine residue of gp120, and the processing is effectively inhibited by an analogue peptide of the cleavage motif (RXK/RR) and by plasmin inhibitors.	Arginine	50-58	plasminogen	Homo sapiens	0-7	
10496984-12	1999	Collectively, our results demonstrate that conformation-dependent arginine-mediated ionic interactions are responsible for the TFPI-2/MSPI triplet binding to fibroblast ECM, heparin, and dermatan sulfate and that heparin augmented the rate of inhibition of plasmin by TFPI-2/MSPI.	Arginine	66-74	plasminogen	Homo sapiens	257-264	
9202057-5	1997	A series of peptides surrounding a plasmin cleavage site (arginine 361) near the carboxy-terminal end of vitronectin were synthesized.	Arginine	58-66	plasminogen	Homo sapiens	35-42	
9798984-5	1998	An average of four of the total nineteen Arg residues in alpha2AP reacted with phenylglyoxal and resulted in complete loss of plasmin inhibitory activity; however, mod alpha2AP competed effectively with native alpha2AP for becoming crosslinked to fibrin by FXIIIa catalysis.	Arginine	41-44	plasminogen	Homo sapiens	126-133	
9572854-0	1998	Arginine 719 in human plasminogen mediates formation of the staphylokinase:plasmin activator complex.	Arginine	0-8	plasminogen	Homo sapiens	22-29	
9253802-0	1997	Effect of L-arginine on in vitro plasmin-generation and fibrinogenolysis.	Arginine	10-20	plasminogen	Homo sapiens	33-40	
9253802-3	1997	The aim of the present paper is to investigate the action of L-arginine on in vitro plasmin generation and fibrino(geno)lysis by chromogenic, kinetic plasmin generation assay and electrophoretic analysis.	Arginine	61-71	plasminogen	Homo sapiens	84-91	
9253802-3	1997	The aim of the present paper is to investigate the action of L-arginine on in vitro plasmin generation and fibrino(geno)lysis by chromogenic, kinetic plasmin generation assay and electrophoretic analysis.	Arginine	61-71	plasminogen	Homo sapiens	150-157	
9253802-4	1997	The acceleration of tPA-induced plasmin generation in the presence of low concentration of L-arginine, along with augmentation of in vitro fibrinogenolysis have been documented.	Arginine	91-101	plasminogen	Homo sapiens	32-39	
1828038-1	1991	Plasmin mainly cleaved the Arg5-Ser6 bond of Arg-Val-Leu-Pro-Arg-interleukin-8 (AVLPR-IL-8) produced by human dermal fibroblasts, which resulted in the conversion of AVLPR-IL-8 to IL-8 and the inactive pentapeptide, though a minor cleavage of AVLPR-IL-8 by plasmin at Lys8-Glu9 bond occurred.	Arginine	27-30	plasminogen	Homo sapiens	0-7	
9169591-6	1997	With the aid of protein engineering, a modified pro-urokinase has been prepared in which the activation sequence normally recognized by plasmin (Pro-Arg-Phe-Lys upward arrowIle-Ile-Gly-Gly) has been replaced by a sequence expected to be recognized and hydrolysed by many MMPs (Arg-Pro-Leu-Gly upward arrowIle-Ile-Gly-Gly).	Arginine	149-152	plasminogen	Homo sapiens	136-143	
8356923-4	1993	PAs specifically hydrolyse a single arginine-valine bond in plasminogen, an abundant and widely distributed plasma zymogen, to form the broad spectrum serine protease, plasmin.	Arginine	36-44	plasminogen	Homo sapiens	60-67	
1531588-6	1992	During digestion of fibrinogen at low plasmin concentration, up to 65% of the FpA was cleaved just subsequent to the progressive release of B beta-(1-42)-peptide, and the Arg-16-Gly-17 bond of the A alpha-chain became relatively stable towards plasmin action when present in fragment E (and possibly fragment Y).	Arginine	171-174	plasminogen	Homo sapiens	38-45	
9132167-1	1996	It has been shown that human growth hormone (hGH) is attacked and digested at Arg(134)-Thr(135) by thrombin and plasmin, facilitating its further degradation in the plasma and tissues.	Arginine	78-81	plasminogen	Homo sapiens	112-119	
1382726-7	1992	Peptides from plasmin digestion of fibronectin containing cell attachment site with sequence Arg-Gly-Asp-Ser and also synthetic peptide reproducing this amino-acid sequence at the concentration of 1000 micrograms/ml released about 50% of collagenase and 55% of elastase from PMN-leukocytes.	Arginine	93-96	plasminogen	Homo sapiens	14-21	
1318546-10	1992	In the only human apo[a] polymorph sequenced to date, position 4308 is occupied by serine, whereas the homologous position in plasmin is occupied by arginine and is an important site for proteolytic cleavage and activation.	Arginine	149-157	plasminogen	Homo sapiens	126-133	
1387746-0	1992	[The effect of arginine on hydrolysis of fibrinogen by plasmin and mini-plasmin].	Arginine	15-23	plasminogen	Homo sapiens	55-62	
1387746-1	1992	The rate of plasmin or Val442-plasmin catalyzed hydrolysis of fibrinogen decreases several times as affected by arginine in high concentrations.	Arginine	112-120	plasminogen	Homo sapiens	12-19	
1387746-1	1992	The rate of plasmin or Val442-plasmin catalyzed hydrolysis of fibrinogen decreases several times as affected by arginine in high concentrations.	Arginine	112-120	plasminogen	Homo sapiens	30-37	
1828038-1	1991	Plasmin mainly cleaved the Arg5-Ser6 bond of Arg-Val-Leu-Pro-Arg-interleukin-8 (AVLPR-IL-8) produced by human dermal fibroblasts, which resulted in the conversion of AVLPR-IL-8 to IL-8 and the inactive pentapeptide, though a minor cleavage of AVLPR-IL-8 by plasmin at Lys8-Glu9 bond occurred.	Arginine	45-48	plasminogen	Homo sapiens	0-7	
1828038-1	1991	Plasmin mainly cleaved the Arg5-Ser6 bond of Arg-Val-Leu-Pro-Arg-interleukin-8 (AVLPR-IL-8) produced by human dermal fibroblasts, which resulted in the conversion of AVLPR-IL-8 to IL-8 and the inactive pentapeptide, though a minor cleavage of AVLPR-IL-8 by plasmin at Lys8-Glu9 bond occurred.	Arginine	45-48	plasminogen	Homo sapiens	257-264	
3315613-7	1987	All of these agents have the same biochemical mechanism of action, cleaving an arginine-valine bond in the plasminogen molecule to form plasmin, but they differ with regard to other important properties.	Arginine	79-87	plasminogen	Homo sapiens	107-114	
34768908-0	2021	Heparin and Arginine Based Plasmin Nanoformulation for Ischemic Stroke Therapy.	Arginine	12-20	plasminogen	Homo sapiens	27-34	
34768908-5	2021	Here in this paper, we report a novel heparin and arginine-based plasmin nanoformulation that exhibits increased plasmin stability and efficacy.	Arginine	50-58	plasminogen	Homo sapiens	65-72	
34768908-5	2021	Here in this paper, we report a novel heparin and arginine-based plasmin nanoformulation that exhibits increased plasmin stability and efficacy.	Arginine	50-58	plasminogen	Homo sapiens	113-120	
2551057-5	1989	Substituting arginine for lysine at the carboxy-terminus or the 17th residue from the carboxy-terminus decreased the affinity of peptides for plasmin 9-fold and 5-fold, respectively, implicating these lysine residues of AP as major ligand sites for plasmin.	Arginine	13-21	plasminogen	Homo sapiens	142-149	
2768221-2	1989	The result has given experimental support to the mechanisms previously proposed by the authors for the selective inhibition of trypsin, thrombin, factor Xa, and plasmin by inhibitors with an arginine or lysine backbone.	Arginine	191-199	plasminogen	Homo sapiens	161-168	
2968979-2	1988	The selective inhibition of trypsin, thrombin, factor Xa, and plasmin exhibited by arginine and lysine derivatives has been clearly explained based on the predicted structure and the homology in the amino acid sequences of these enzymes.	Arginine	83-91	plasminogen	Homo sapiens	62-69	
2954262-1	1987	The relationship between chemical modifications of arginine derivatives and inhibitory activity to trypsin, plasmin and glandular kallikrein was investigated comparing with that of thrombin and concluded as follows: The hydrophobic binding pocket, which has been reported previously to be stereogeometrically very similar in trypsin and thrombin, corresponded to the length of ethylpiperidine.	Arginine	51-59	plasminogen	Homo sapiens	108-115	
6197164-1	1984	The plasminogen activators of surgically excised prostate cancers (43 specimens) and benign prostatic hyperplasias (33 specimens) were extracted with an acetate:arginine:detergent buffer, and the activities were quantitated with azocaseinolytic tests.	Arginine	161-169	plasminogen	Homo sapiens	4-15	
2933077-2	1985	Values of kinetic parameters for the hydrolysis of esters and p-nitroanilides of L-lysine and L-arginine catalyzed by the Lys77 form of human plasmin (EC 3.4.21.7) have been determined between pH 5.5 and 8 (I = 0.1 M) at 21 +/- 0.5 degrees C. Over the whole pH range explored, Lys77-plasmin catalysis conforms to simple Michaelis-Menten kinetics, and steady-state and pre-steady-state data may be consistently fitted to the minimum three-step mechanism: E + S in equilibrium (k+1/k-1)E X S----(k+2)E X P + P1----(k+3)E + P2 In spite of the higher specificity of lysyl derivatives for Lys77-plasmin rather than the arginyl ones, kinetic parameters also depend on the nature of the N-alpha substituent and/or of the alcoholic or p-nitroanilidic moiety of the substrate.	Arginine	94-104	plasminogen	Homo sapiens	142-149	
2933077-2	1985	Values of kinetic parameters for the hydrolysis of esters and p-nitroanilides of L-lysine and L-arginine catalyzed by the Lys77 form of human plasmin (EC 3.4.21.7) have been determined between pH 5.5 and 8 (I = 0.1 M) at 21 +/- 0.5 degrees C. Over the whole pH range explored, Lys77-plasmin catalysis conforms to simple Michaelis-Menten kinetics, and steady-state and pre-steady-state data may be consistently fitted to the minimum three-step mechanism: E + S in equilibrium (k+1/k-1)E X S----(k+2)E X P + P1----(k+3)E + P2 In spite of the higher specificity of lysyl derivatives for Lys77-plasmin rather than the arginyl ones, kinetic parameters also depend on the nature of the N-alpha substituent and/or of the alcoholic or p-nitroanilidic moiety of the substrate.	Arginine	94-104	plasminogen	Homo sapiens	283-290	
2933077-2	1985	Values of kinetic parameters for the hydrolysis of esters and p-nitroanilides of L-lysine and L-arginine catalyzed by the Lys77 form of human plasmin (EC 3.4.21.7) have been determined between pH 5.5 and 8 (I = 0.1 M) at 21 +/- 0.5 degrees C. Over the whole pH range explored, Lys77-plasmin catalysis conforms to simple Michaelis-Menten kinetics, and steady-state and pre-steady-state data may be consistently fitted to the minimum three-step mechanism: E + S in equilibrium (k+1/k-1)E X S----(k+2)E X P + P1----(k+3)E + P2 In spite of the higher specificity of lysyl derivatives for Lys77-plasmin rather than the arginyl ones, kinetic parameters also depend on the nature of the N-alpha substituent and/or of the alcoholic or p-nitroanilidic moiety of the substrate.	Arginine	94-104	plasminogen	Homo sapiens	283-290	
2932824-4	1985	Benzamidine-binding sites of domain K5 and of plasmin light chain are simultaneously arginine-binding ones.	Arginine	85-93	plasminogen	Homo sapiens	46-53	
6449829-3	1980	This substance, designated "plasmin", was separated from plasmin and kallikrein in a three-step procedure using columns of lysine-Sepharose, DEAE-Sephadex A-50, and arginine-Sepharose.	Arginine	165-173	plasminogen	Homo sapiens	28-35	
6448971-3	1980	Comparative experiences with the same substrate revealed that carboxypeptidase B liberated exclusively the C-terminal arginine, plasmin exclusively peptides of arginine, and trypsin, besides arginine peptides, minutes quantities of free arginine.	Arginine	118-126	plasminogen	Homo sapiens	128-135	
6448971-3	1980	Comparative experiences with the same substrate revealed that carboxypeptidase B liberated exclusively the C-terminal arginine, plasmin exclusively peptides of arginine, and trypsin, besides arginine peptides, minutes quantities of free arginine.	Arginine	160-168	plasminogen	Homo sapiens	128-135	
6448971-3	1980	Comparative experiences with the same substrate revealed that carboxypeptidase B liberated exclusively the C-terminal arginine, plasmin exclusively peptides of arginine, and trypsin, besides arginine peptides, minutes quantities of free arginine.	Arginine	160-168	plasminogen	Homo sapiens	128-135	
4229624-0	1966	[Activity of plasmin and streptokinase-activator on substituted arginine and lysine esters].	Arginine	64-72	plasminogen	Homo sapiens	13-20